Lipid-fosfatna fosfataza

Lipid-fosfatna fosfataza
Identifikatori
EC broj 3.1.3.76
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
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PMC articles
PubMed articles
NCBI Protein search

Lipid-fosfatna fosfataza (EC 3.1.3.76, hidroksi masno kiselinska fosfataza, dihidroksi masno kiselinska fosfataza, hidroksi lipidna fosfataza, sEH, hidrolaza rastvornog epoksida) je enzim sa sistematskim imenom (9S,10S)-10-hidroksi-9-(fosfonooksi)oktadekanoat fosfohidrolaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju

(9S,10S)-10-hidroksi-9-(fosfonooksi)oktadekanoat + H2O ⇌ {\displaystyle \rightleftharpoons } (9S,10S)-9,10-dihidroksioktadekanoat + fosfat

Za rad ovog enzim je neophodan Mg2+.

Reference

  1. ↑ Newman, J.W., Morisseau, C., Harris, T.R. and Hammock, B.D. (2003). „The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity”. Proc. Natl. Acad. Sci. USA 100: 1558-1563. PMID 12574510. 
  2. ↑ Cronin, A., Mowbray, S., Dürk, H., Homburg, S., Fleming, I., Fisslthaler, B., Oesch, F. and Arand, M. (2003). „The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase”. Proc. Natl. Acad. Sci. USA 100: 1552-1557. PMID 12574508. 
  3. ↑ Morisseau, C. and Hammock, B.D. (2005). „Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles”. Annu. Rev. Pharmacol. Toxicol. 45: 311-333. PMID 15822179. 
  4. ↑ Tran, K.L., Aronov, P.A., Tanaka, H., Newman, J.W., Hammock, B.D. and Morisseau, C. (2005). „Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase”. Biochemistry 44: 12179-12187. PMID 16142916. 
  5. ↑ Newman, J.W., Morisseau, C. and Hammock, B.D. (2005). „Epoxide hydrolases: their roles and interactions with lipid metabolism”. Prog. Lipid Res. 44: 1-51. PMID 15748653. 
  6. ↑ Srivastava, P.K., Sharma, V.K., Kalonia, D.S. and Grant, D.F. (2004). „Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure”. Arch. Biochem. Biophys. 427: 164-169. PMID 15196990. 
  7. ↑ Gomez, G.A., Morisseau, C., Hammock, B.D. and Christianson, D.W. (2004). „Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis”. Biochemistry 43: 4716-4723. PMID 15096040. 

Literatura

  • Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
  • Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
  • Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 

Spoljašnje veze

  • MeSH Lipid-phosphate+phosphatase
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TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6